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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2000-12-20
pubmed:abstractText
Previous studies have shown that the motility of flagellar and ciliary axonemes in many organisms are influenced by the concentration of both ATP and ADP. Detergent-extracted cell models of Chlamydomonas oda1, a mutant lacking flagellar outer-arm dynein, displayed slightly lower flagellar beating frequencies when reactivated with ATP in the presence of an ATP-regenerating system, composed of creatine phosphate and creatine phosphokinase, than when reactivated with ATP alone. Thus, presence of a low concentration of ADP may somehow stimulate axonemal motility. To see if this motility stimulation is due to a direct effect on dynein, we analyzed the effect of ADP on the in vitro microtubule translocation caused by isolated inner-arm dyneins in the presence of ATP. Of the seven inner-arm dyneins (species a-g) fractionated by ion-exchange chromatography, most species translocated microtubules at faster speed in the presence of 0.1 mM ATP and 0.1 mM ADP than in the presence of 0.1 mM ATP alone. Most notably, species a and e did not translocate microtubules at all in the presence of the ATP-regenerating system, indicating that a trace amount of ADP is necessary for their motility. This regulation may be effected through binding of ADP to some of the four nucleotide binding sites in each dynein heavy chain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0386-7196
pubmed:author
pubmed:issnType
Print
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
263-7
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
ADP-dependent microtubule translocation by flagellar inner-arm dyneins.
pubmed:affiliation
Department of Biological Sciences, Graduate School of Science, University of Tokyo, Japan. yagt@biol.s.u-tokyo.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't